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Xylella fastidiosa Esterase Rather than Hydroxynitrile Lyase
Author(s) -
Torrelo Guzman,
Ribeiro de Souza Fayene Zeferino,
Carrilho Emanuel,
Hanefeld Ulf
Publication year - 2015
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201402685
Subject(s) - xylella fastidiosa , homology modeling , biochemistry , esterase , biology , active site , enzyme , lyase , hydrolase , docking (animal) , chemistry , stereochemistry , genetics , bacteria , medicine , nursing
In 2009, we reported that the product of the gene SCJ21.16 (XFa0032) from Xylella fastidiosa , a xylem‐restricted plant pathogen that causes a range of diseases in several important crops, encodes a protein ( Xf HNL) with putative hydroxynitrile lyase activity. Sequence analysis and activity tests indicated that Xf HNL exhibits an α/β‐hydrolase fold and could be classified as a member of the family of FAD‐independent HNLs. Here we provide a more detailed sequence analysis and new experimental data. Using pure heterologously expressed Xf HNL we show that this enzyme cannot catalyse the cleavage/synthesis of mandelonitrile and that this protein is in fact a non‐enantioselective esterase. Homology modelling and ligand docking simulations were used to study the active site and support these results. This finding could help elucidate the common ancestor of esterases and hydroxynitrile lyases with an α/β ‐hydrolase fold.